Journal: Journal of Clinical Medicine

Article Title: Moderate Aerobic Exercise Regulates Follicular Dysfunction by Initiating Brain-Derived Neurotrophic Factor (BDNF)-Mediated Anti-Apoptotic Signaling Pathways in Polycystic Ovary Syndrome

doi: 10.3390/jcm11195584

Figure Lengend Snippet: Sequences of primers designed for RT-qPCR.

Article Snippet: Sections were incubated overnight at 4 °C with antibodies against BDNF (1:100, Wanleibio), TrkB (1:100, Wanleibio), p75NTR (1:100, 55014-1-AP, Proteintech, Chicago, IL, USA), and Cleaved-Caspase-3 (1:100, 66470-2-Ig, Proteintech) at a 1:100 dilution.

Techniques:

Journal: Journal of Clinical Medicine

Article Title: Moderate Aerobic Exercise Regulates Follicular Dysfunction by Initiating Brain-Derived Neurotrophic Factor (BDNF)-Mediated Anti-Apoptotic Signaling Pathways in Polycystic Ovary Syndrome

doi: 10.3390/jcm11195584

Figure Lengend Snippet: The expression of BDNF, TrkB, and p75NTR in ovarian follicles of PCOS rats after aerobic exercise. Rats received DHEA for the induction of polycystic ovarian syndrome, together with or without exercise treatment. ( A , B ) The expression levels of BDNF in ovarian follicles at different stages were analyzed by immunohistochemistry. ( C , D ) The expression levels of BDNF in ovarian follicles were analyzed by immunofluorescence. ( E , F ) The co-expression of TrkB and p75NTR in ovarian follicles at different stages was detected by immunofluorescence double labeling. n = 10 in each group. Data are shown as mean ± SEM. ** p < 0.05, vs. control group; ## p < 0.01, vs. PCOS group.

Article Snippet: Sections were incubated overnight at 4 °C with antibodies against BDNF (1:100, Wanleibio), TrkB (1:100, Wanleibio), p75NTR (1:100, 55014-1-AP, Proteintech, Chicago, IL, USA), and Cleaved-Caspase-3 (1:100, 66470-2-Ig, Proteintech) at a 1:100 dilution.

Techniques: Expressing, Immunohistochemistry, Immunofluorescence, Labeling, Control

Journal: Journal of Clinical Medicine

Article Title: Moderate Aerobic Exercise Regulates Follicular Dysfunction by Initiating Brain-Derived Neurotrophic Factor (BDNF)-Mediated Anti-Apoptotic Signaling Pathways in Polycystic Ovary Syndrome

doi: 10.3390/jcm11195584

Figure Lengend Snippet: Aerobic exercise activated BDNF signaling in the ovary of DHEA-induced PCOS rats. Rats received DHEA for the induction of polycystic ovarian syndrome, together with or without exercise treatment. ( A ) mRNA expression of BDNF, TrkB, and p75NTR factors in ovarian tissue was analyzed by real-time PCR. ( B , C ) The expression of BDNF, TrkB, and p75NTR in ovarian tissue was assessed by Western blot assay. ( D , E ) The expression of PI3K, AKT, and p-AKT in ovarian tissue was assessed by Western blot assay. ( F – I ) The expression of p75NTR, NF-κB, p-NF-κB, JNK, and p-JNK in ovarian tissue was assessed by Western blot assay. n = 10 in each group. Data are shown as mean ± SEM. ** p < 0.05, vs. control group; ## p < 0.01, vs. PCOS group.

Article Snippet: Sections were incubated overnight at 4 °C with antibodies against BDNF (1:100, Wanleibio), TrkB (1:100, Wanleibio), p75NTR (1:100, 55014-1-AP, Proteintech, Chicago, IL, USA), and Cleaved-Caspase-3 (1:100, 66470-2-Ig, Proteintech) at a 1:100 dilution.

Techniques: Expressing, Real-time Polymerase Chain Reaction, Western Blot, Control

Journal: Frontiers in Molecular Biosciences

Article Title: USF1 Transcriptionally Regulates UGT1A3 and Promotes Lung Adenocarcinoma Progression by Regulating Neurotrophin Signaling Pathway

doi: 10.3389/fmolb.2022.758968

Figure Lengend Snippet: Knockdown of USF1 inhibited cells proliferation, migration and invasion via deregulation of the neurotrophin signaling pathway. (A) The protein expression of p75NTR, RIPK2, IRAK1, IKKβ and USF1, detected by WB in H1299 and A549 cells; (B) The levels of IRAK1 was detected by WB in H1299 and A549 cells; (C,D) Cells migration was detected by wound healing assay in H1299 and A549 cells; (E,F) Cells migration and invasion were detected by transwell assay in H1299 and A549 cells; (The sh-USF1, cells were transfected with sh-USF1; sh-USF1+pcDNA3.1, cells were transfected with sh-USF1 and pcDNA3.1; sh-USF1+ pcDNA3.1- IRAK1; * p < .05 means statistically significant difference when compared with sh-USF1+ pcDNA3.1 group).

Article Snippet: After that, membranes were incubated overnight at 4°C with rabbit polyclonal antibody anti-USF1 (abs115735, 1:500 dilution, Absin, Shanghai, China), rabbit UGT1A3 polyclonal antibody (H00054659-A01, 1:500 dilution, Abnova, Wuhan, China), and rabbit P75 neurotrophic factor receptor (P75NTR) polyclonal antibody (TA328682, 1:200 dilution, OriGene Technologies, Rockville, United States), rabbit receptor interacting serine/threonine kinase 2 (RIPK2) polyclonal antibody (abs130017, 1:500 dilution, Absin, Shanghai, China), rabbit interleukin-1 receptor-associated kinase 1 (IRAK1) polyclonal antibody (AF7290, 1:500 dilution, Beyotime Biotechnology, Shanghai, China), rabbit ikappaB kinase β (IKKβ) polyclonal antibody (AF7200, 1:300 dilution, Beyotime Biotechnology, Shanghai, China), while the rabbit anti-GAPDH polyclonal antibody (1:500, Cell Signaling Technology, Inc.; Shangahi, China) was used as a control.

Techniques: Knockdown, Migration, Expressing, Wound Healing Assay, Transwell Assay, Transfection

Journal:

Article Title: Detergent-insoluble GPI-anchored Proteins Are Apically Sorted in Fischer Rat Thyroid Cells, but Interference with Cholesterol or Sphingolipids Differentially Affects Detergent Insolubility and Apical Sorting

doi:

Figure Lengend Snippet: Steady-state distribution and delivery to the plasma membrane of PLAP and NTR-PLAP in transfected FRT cells. (A) Schemes of PLAP and NTR-PLAP (a fusion protein containing the ectodomain of p75NTR and the C-terminal GPI attachment signal of PLAP). (B) FRT cells stably expressing PLAP or NTR-PLAP were grown to confluence and pulsed overnight with [35S]met–cys or [35S]cys, respectively. After surface biotinylation from the apical (Ap) and basolateral (BL) domains, cells were lysed, immunoprecipitated against specific antibodies, and reprecipitated against streptavidin. (C) FRT cells were labeled for 20 min with [35S]met–cys or [35S]cys. At different times of the chase, surface proteins were biotinylated from the apical (Ap) or the basolateral (BL) side. Cells were then lysed and immunoprecipitated with antibodies against PLAP or NTR and with streptavidin beads. Samples were run on 10% SDS-PAGE and detected by fluorography. PLAP and NTR-PLAP are directly sorted to the apical surface in FRT cells, whereas a small percentage of the two proteins is delivered with similar kinetics to the basolateral domain.

Article Snippet: The polyclonal antibody against PLAP was from Rockland (Gilbertsville, PA), and anti-p75NTR mAb was a gift from Andrè Le Bivic (Institut de Biologie du Développement de Marseille, Marseille, France).

Techniques: Transfection, Stable Transfection, Expressing, Immunoprecipitation, Labeling, SDS Page

Journal:

Article Title: Detergent-insoluble GPI-anchored Proteins Are Apically Sorted in Fischer Rat Thyroid Cells, but Interference with Cholesterol or Sphingolipids Differentially Affects Detergent Insolubility and Apical Sorting

doi:

Figure Lengend Snippet: Pulse-chase analysis and purification on sucrose gradients of transmembrane forms of PLAP and p75NTR in transfected FRT cells. (A) Schemes of p75NTR and PLAP-PS321 (a fusion protein containing the ectodomain of PLAP and the transmembrane and the cytoplasmic domain of the PS321 NTR mutant). (B) Pulse-chase and TX-100 extraction of p75NTR and PLAP-PS321. FRT cells expressing p75NTR and PLAP-PS321 were labeled with [35S]cys or [35S]met–cys, respectively, and subsequently treated as described in Figure ​Figure2A.2A. (C) Purification of p75NTR- and PLAP-PS321–enriched fractions on sucrose density gradients. Labeled proteins of FRT cells expressing p75NTR and PLAP-PS321 were solubilized in TX-100 and purified as described in Figure ​Figure2B.2B. Both transmembrane proteins are soluble in TX-100 and do not float on sucrose density gradients.

Article Snippet: The polyclonal antibody against PLAP was from Rockland (Gilbertsville, PA), and anti-p75NTR mAb was a gift from Andrè Le Bivic (Institut de Biologie du Développement de Marseille, Marseille, France).

Techniques: Pulse Chase, Purification, Transfection, Mutagenesis, Expressing, Labeling

Journal:

Article Title: Detergent-insoluble GPI-anchored Proteins Are Apically Sorted in Fischer Rat Thyroid Cells, but Interference with Cholesterol or Sphingolipids Differentially Affects Detergent Insolubility and Apical Sorting

doi:

Figure Lengend Snippet: Surface expression of GPI-anchored, secretory, and transmembrane proteins after FB1 treatment. (A) FRT cells stably expressing PLAP, NTR-PLAP, or gD1-DAF were grown to confluence in the absence (−) or presence (+) of FB1, as described in MATERIALS AND METHODS. After 30 min of labeling with [35S]met–cys or [35S]cys and a 2-h chase, cells were surface biotinylated from the apical (Ap) or the basolateral (BL) domain, lysed, immunoprecipitated against specific antibodies, and reprecipitated against streptavidin. (B) Amounts of labeled proteins were quantified from three independent experiments and are shown as means ± SD. Hatched bars represent apical proteins, and black bars represent basolateral proteins. Apical PLAP and NTR-PLAP, but not basolateral gD1-DAF, became unpolarized after FB1 treatment. (C) FRT cells expressing PLAP-sec, NTR-sec, p75NTR, or PLAP-PS321 were grown to confluence in the absence (−) or presence (+) of FB1, as described in MATERIALS AND METHODS. After labeling with [35S]met–cys or [35S]cys for 20 min and a chase of 2 h, apical and basolateral media were collected separately and cells were surface biotinylated from apical or basolateral domains. Polarized secretion of the secretory forms was revealed by immunoprecipitation in the apical and basolateral medium (top two panels), whereas biotinylated transmembrane proteins were revealed by double immunoprecipitation with specific antibody and streptavidin beads (bottom two panels). (D) Amounts of labeled proteins were quantified from three independent experiments and are shown as means ± SD. Hatched bars represent apical proteins, and black bars represent basolateral proteins. FB1 does not alter the sorting of transmembrane and secretory proteins.

Article Snippet: The polyclonal antibody against PLAP was from Rockland (Gilbertsville, PA), and anti-p75NTR mAb was a gift from Andrè Le Bivic (Institut de Biologie du Développement de Marseille, Marseille, France).

Techniques: Expressing, Stable Transfection, Labeling, Immunoprecipitation

Journal:

Article Title: Detergent-insoluble GPI-anchored Proteins Are Apically Sorted in Fischer Rat Thyroid Cells, but Interference with Cholesterol or Sphingolipids Differentially Affects Detergent Insolubility and Apical Sorting

doi:

Figure Lengend Snippet: Surface expression of GPI-anchored and transmembrane proteins after cholesterol depletion. (A) FRT cells expressing PLAP, NTR-PLAP, gD1-DAF, p75NTR, or PLAP-PS321 were grown on filters and treated with mevinolin (Mev.; 10 μM) for 48 h and M-β-CD (10 mM) for 60 min. Cells were then pulse labeled for 30 min, chased for 2 h, and biotinylated as usual. (B) Amounts of labeled proteins were quantified in three independent experiments and are shown as means ± SD. Hatched bars represent apical (Ap) proteins, and black bars represent basolateral (BL) proteins. Removal of cholesterol does not alter the surface expression of apical and basolateral GPI-anchored and transmembrane proteins.

Article Snippet: The polyclonal antibody against PLAP was from Rockland (Gilbertsville, PA), and anti-p75NTR mAb was a gift from Andrè Le Bivic (Institut de Biologie du Développement de Marseille, Marseille, France).

Techniques: Expressing, Labeling

Journal: Experimental and Therapeutic Medicine

Article Title: Formation of three-dimensional cell aggregates expressing lens-specific proteins in various cultures of human iris-derived tissue cells and iPS cells

doi: 10.3892/etm.2022.11476

Figure Lengend Snippet: Induction of differentiation using the Ex.1 method. (A) Colony of human iris-derived iPS cells. (B-D) Cell colony in differentiation culture: (B) 6th day in STEP-1 medium, (C) 18th day in STEP-2 medium, and (D) 25th day in STEP-3 medium. Scale bar in (A-D), 100 µm. (E) Fold-increase in p75NTR mRNA expression level at different steps relative to STEP-0: * P<0.05. (F) Cell morphology on 35th day of differentiation in STEP-3 medium. (G) Immunostaining for αA-crystallin in the same area as indicated in (F). (H) Immunostaining for SOX2 in the same area as in (G). (I) Merged image of αA-crystallin and SOX2 immunostaining. Scale bar in (F-I), 100 µm. Ex, experiment; iPS cells, induced pluripotent stem cells.

Article Snippet: Briefly, fixed cells were permeabilized with 0.5% Triton X-100 (cat. no. 04605-250; FUJIFILM Wako), blocked with a serum-free ready-to-use blocking reagent (cat. no. X090930-2; Agilent Technologies, Inc.) for 5 min at room temperature, and stained with one of the following primary antibodies (incubated for 1 h at 37˚C): anti-human αA-crystallin rabbit polyclonal antibody (1:100; cat. no. ab5595; Abcam plc.), anti-human PAX6 mouse monoclonal antibody (1:100; cat. no. 14-9914-80; Thermo Fisher Scientific), anti-human SOX2 rat monoclonal antibody (1:100; cat. no. 14-9811-82; Thermo Fisher Scientific), anti-human type IV collagen rabbit polyclonal antibody (1:200; cat. no. LB-0445; Life Science Laboratories, Inc.), anti-p75NTR rabbit polyclonal antibody (1:200; cat. no. ANT-007; Alomone Labs), and anti-human βB2-crystallin rabbit polyclonal antibody (1:100; cat. no. ab252971; Abcam).

Techniques: Derivative Assay, Expressing, Immunostaining

Journal: Experimental and Therapeutic Medicine

Article Title: Formation of three-dimensional cell aggregates expressing lens-specific proteins in various cultures of human iris-derived tissue cells and iPS cells

doi: 10.3892/etm.2022.11476

Figure Lengend Snippet: Changes in gene expression levels at each step of differentiation induction using Ex.4 the method. (A) SOX2 , (B) PAX6 , (C) p75NTR , (D) αA-crystallin , (E) type-IV collagen ; fold-changes are relative to gene expression level in STEP-0: * P<0.05, ** P<0.01, *** P<0.005. Ex, experiment.

Article Snippet: Briefly, fixed cells were permeabilized with 0.5% Triton X-100 (cat. no. 04605-250; FUJIFILM Wako), blocked with a serum-free ready-to-use blocking reagent (cat. no. X090930-2; Agilent Technologies, Inc.) for 5 min at room temperature, and stained with one of the following primary antibodies (incubated for 1 h at 37˚C): anti-human αA-crystallin rabbit polyclonal antibody (1:100; cat. no. ab5595; Abcam plc.), anti-human PAX6 mouse monoclonal antibody (1:100; cat. no. 14-9914-80; Thermo Fisher Scientific), anti-human SOX2 rat monoclonal antibody (1:100; cat. no. 14-9811-82; Thermo Fisher Scientific), anti-human type IV collagen rabbit polyclonal antibody (1:200; cat. no. LB-0445; Life Science Laboratories, Inc.), anti-p75NTR rabbit polyclonal antibody (1:200; cat. no. ANT-007; Alomone Labs), and anti-human βB2-crystallin rabbit polyclonal antibody (1:100; cat. no. ab252971; Abcam).

Techniques: Expressing

Journal: Experimental and Therapeutic Medicine

Article Title: Formation of three-dimensional cell aggregates expressing lens-specific proteins in various cultures of human iris-derived tissue cells and iPS cells

doi: 10.3892/etm.2022.11476

Figure Lengend Snippet: Induction of differentiation using the Ex.4 method. (A) Gross observation of cell aggregate. Reduced opacity is observed in certain areas. Scale bar, 2 mm. (B) H&E-stained specimen of cell aggregate. Scale bar, 200 µm. (C) Enlarged view of H&E staining in Area 1 of the specimen in (B). Cells displaying epithelial-like morphology have infiltrated inside the cell aggregate (yellow arrowhead). (D-G and I-L) Immunostaining of cell aggregates for (D and I) SOX2, (E and J) p75NTR, (F and K) αA-crystallin, and (G and L) type IV collagen. Blue in immunostaining images: DAPI staining of nuclei. (H) Enlarged view of H&E staining of Area 2 in the specimen in (B), where the cells on the surface of the aggregate have transitioned from a multilayer to a monolayer (white arrowhead). Scale bar in (C-L), 50 µm. Ex, experiment; H&E, hematoxylin and eosin.

Article Snippet: Briefly, fixed cells were permeabilized with 0.5% Triton X-100 (cat. no. 04605-250; FUJIFILM Wako), blocked with a serum-free ready-to-use blocking reagent (cat. no. X090930-2; Agilent Technologies, Inc.) for 5 min at room temperature, and stained with one of the following primary antibodies (incubated for 1 h at 37˚C): anti-human αA-crystallin rabbit polyclonal antibody (1:100; cat. no. ab5595; Abcam plc.), anti-human PAX6 mouse monoclonal antibody (1:100; cat. no. 14-9914-80; Thermo Fisher Scientific), anti-human SOX2 rat monoclonal antibody (1:100; cat. no. 14-9811-82; Thermo Fisher Scientific), anti-human type IV collagen rabbit polyclonal antibody (1:200; cat. no. LB-0445; Life Science Laboratories, Inc.), anti-p75NTR rabbit polyclonal antibody (1:200; cat. no. ANT-007; Alomone Labs), and anti-human βB2-crystallin rabbit polyclonal antibody (1:100; cat. no. ab252971; Abcam).

Techniques: Staining, Immunostaining

Journal: Cell reports

Article Title: Macrophage memories of early-life injury drive neonatal nociceptive priming

doi: 10.1016/j.celrep.2024.114129

Figure Lengend Snippet: KEY RESOURCES TABLE

Article Snippet: siRNA against p75NTR – Human , Origene , SR321107.

Techniques: Recombinant

Journal: Biomedicines

Article Title: p75NTR Modulation Reduces Oxidative Stress and the Expression of Pro-Inflammatory Mediators in a Cell Model of Rett Syndrome

doi: 10.3390/biomedicines12112624

Figure Lengend Snippet: Expression of NGF and p75NTR fibroblasts derived from control individuals and Rett patients. ( A ) Total RNA was extracted from healthy control (HC-1) and Rett syndrome (RTT-1) fibroblasts, and the expression levels of ngf were measured by qRT-PCR. n = 3 biological replicates. Data represent means ± SD. ( B ) Immunofluorescence and respective quantitative analysis of NGF in HC and RTT. Cells were fixed in 4% PFA and stained with antibodies against NGF (red). DAPI (blue) was employed for nuclear counterstaining. n = 6 biological replicates. ( C ) qRT-PCR analysis of ngfr ( p75NTR ) in HC-1 and RTT-1 fibroblasts. n = 3 biological replicates. ( D ) Immunofluorescence and respective quantitative analysis of p75NTR immunoreactivity in HC-1 and RTT-1 cells. Cells were fixed in 4% PFA and stained with anti-p75NTR (red). DAPI (blue) was used to counterstain nuclei. n = 5 biological replicates. Data are expressed as mean ± SD. Statistical analysis was performed by using the Student’s unpaired t -test. Statistical significance is indicated as follows: * p < 0.05; ** p < 0.01; *** p < 0.001 vs. DMSO. Images were acquired using the Leica TCS SP8 confocal microscope and Leica Application Suite X (LAS X) software at 40× magnification. Scale bar: 50 µm.

Article Snippet: The anti-NGF and anti-p75NTR antibodies were validated using NGF (BLP-N240, Alomone labs, Jerusalem, Israel) and p75NTR (BLP-NT011 Alomone labs, Jerusalem, Israel) blocking peptides.

Techniques: Expressing, Derivative Assay, Control, Quantitative RT-PCR, Immunofluorescence, Staining, Microscopy, Software

Journal: Biomedicines

Article Title: p75NTR Modulation Reduces Oxidative Stress and the Expression of Pro-Inflammatory Mediators in a Cell Model of Rett Syndrome

doi: 10.3390/biomedicines12112624

Figure Lengend Snippet: Effects of p75NTR modulation on the antioxidant response in RTT fibroblasts. Representative Western blot and densitometric analysis of ( A ) SOD1, ( B ) SOD2, ( C ) Catalase, ( D ) TrxR1, and ( E ) Gpx1 in healthy control fibroblasts (HC-1), Rett syndrome fibroblasts (RTT-1) and RTT fibroblasts treated with 0.1 μM of LM11A-31(RTT-1+LM) for 24 h. n = 3–5 biological replicates. GAPDH was used as a loading control. ( F ) Immunofluorescence and quantification of GSH immunoreactivity in HC-1, RTT-1, and RTT-1+LM experimental groups. Cells were fixed in 4% PFA and stained with antibodies against GSH (red). Nuclear staining was performed with DAPI (blue). n = 12 biological replicates. Data are expressed as mean ± SD. Statistical analysis was performed using one-way ANOVA, followed by Tukey’s post hoc test. Statistical significance is indicated as follows: ** p < 0.01; *** p < 0.001. “a” indicates statistical significance vs. HC-1; “b” indicates statistical significance vs. RTT-1. Images were acquired using the Leica TCS SP8 confocal microscope and Leica Application Suite X (LAS X) software at 40× magnification. Scale bar: 50 µm.

Article Snippet: The anti-NGF and anti-p75NTR antibodies were validated using NGF (BLP-N240, Alomone labs, Jerusalem, Israel) and p75NTR (BLP-NT011 Alomone labs, Jerusalem, Israel) blocking peptides.

Techniques: Western Blot, Control, Immunofluorescence, Staining, Microscopy, Software

Journal: Biomedicines

Article Title: p75NTR Modulation Reduces Oxidative Stress and the Expression of Pro-Inflammatory Mediators in a Cell Model of Rett Syndrome

doi: 10.3390/biomedicines12112624

Figure Lengend Snippet: p75NTR modulation reduces IL-6 and IL-8 expression in RTT fibroblasts. Representative immunofluorescence and respective quantitative analysis of ( A ) IL-6 immunoreactivity in control fibroblasts (HC-1), Rett syndrome fibroblasts (RTT-1), and RTT fibroblasts treated with LM11A-31(RTT-1+LM) at the dose of 0.1 μM for 24 h. Cells were fixed in 4% PFA and stained with antibodies against IL-6 (red). DAPI was used to counterstain nuclei. n = 6 biological replicates. Images were acquired using the Leica TCS SP8 confocal microscope and Leica Application Suite X (LAS X) software at 40× magnification. Scale bar: 50 µm. ( B ) ELISA on IL-6 in culture medium from HC-1, RTT-1, and RTT-1+LM groups treated as abovementioned. n = 4 biological replicates. ( C ) IL-8 immunoreactivity (red) and respective quantitative analysis performed on HC-1, RTT-1, and RTT-1+LM fibroblasts treated as in ( A ). DAPI was used for nuclear staining. n = 6 biological replicates. Scale bar: 50 µm. ( D ) ELISA on secreted IL-8 in conditioned medium from HC-1, RTT-1, and RTT-1+LM cells treated as abovementioned. n = 4 biological replicates. Data are expressed as mean ± SD. Statistical analysis was performed using one-way ANOVA, followed by Tukey’s post hoc test. Statistical significance is indicated as follows: * p < 0.05; ** p < 0.01; *** p < 0.001. “a” indicates statistical significance vs. HC-1; “b” indicates statistical significance vs. RTT-1.

Article Snippet: The anti-NGF and anti-p75NTR antibodies were validated using NGF (BLP-N240, Alomone labs, Jerusalem, Israel) and p75NTR (BLP-NT011 Alomone labs, Jerusalem, Israel) blocking peptides.

Techniques: Expressing, Immunofluorescence, Control, Staining, Microscopy, Software, Enzyme-linked Immunosorbent Assay